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Conserved domains on  [gi|738449907|ref|WP_036401092|]
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MULTISPECIES: retroviral-like aspartic protease family protein [Microcystis]

Protein Classification

pepsin/retropepsin-like aspartic protease family protein( domain architecture ID 27721)

pepsin/retropepsin-like aspartic protease family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5550 super family cl42565
Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];
10-137 3.44e-15

Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5550:

Pssm-ID: 444293  Cd Length: 117  Bit Score: 67.21  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738449907  10 DMGKIYTSITVINRADQilaaaavispdqiRSLTLEnVLVDTGATT-LCLVPEVISRLGLQLLKEVDVATAKGIGKARIF 88
Cdd:COG5550    3 IMGEAFVEVEVIRLPDG-------------ESLEVD-ALVDTGFTGfLVLPSQLIEELGLPELGRRRARLADGSEVEFDV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 738449907  89 RDATLIIAGREGTFECLELPGGQNNLLGVIPLEALGLEPDLLSQKLRVL 137
Cdd:COG5550   69 YEATIEWDGQEAEVPVLAGDGITEPLLGVALLEGLGLVVDPIEGGLVLI 117
 
Name Accession Description Interval E-value
COG5550 COG5550
Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];
10-137 3.44e-15

Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444293  Cd Length: 117  Bit Score: 67.21  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738449907  10 DMGKIYTSITVINRADQilaaaavispdqiRSLTLEnVLVDTGATT-LCLVPEVISRLGLQLLKEVDVATAKGIGKARIF 88
Cdd:COG5550    3 IMGEAFVEVEVIRLPDG-------------ESLEVD-ALVDTGFTGfLVLPSQLIEELGLPELGRRRARLADGSEVEFDV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 738449907  89 RDATLIIAGREGTFECLELPGGQNNLLGVIPLEALGLEPDLLSQKLRVL 137
Cdd:COG5550   69 YEATIEWDGQEAEVPVLAGDGITEPLLGVALLEGLGLVVDPIEGGLVLI 117
clan_AA_DTGF TIGR03698
clan AA aspartic protease, AF_0612 family; Members of this protein family are clan AA aspartic ...
 33-134 5.39e-09

clan AA aspartic protease, AF_0612 family; Members of this protein family are clan AA aspartic proteases, related to family TIGR02281. These proteins resemble retropepsins, pepsin-like proteases of retroviruses such as HIV. Members of this family are found in archaea and bacteria. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163410  Cd Length: 107  Bit Score: 50.82  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738449907   33 VISPDQIRSLTLeNVLVDTGATTLCLVP-EVISRLGLQLLKEVDVATAkgIGKARIFR--DATLIIAGREGTFECLELPG 109
Cdd:TIGR03698   6 LSNPKNPEFMEV-RALVDTGFSGFLLVPpDIVNKLGLPELDQRRVYLA--DGREVLTDvaKASIIINGLEIDAFVESLGY 82

                          90       100
                  ....*....|....*....|....*
gi 738449907  110 GQNNLLGVIPLEALGLEPDLLSQKL 134
Cdd:TIGR03698  83 VDEPLLGTELLEGLGIVIDYRNQGL 107
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 47-116 2.99e-03

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 35.00  E-value: 2.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738449907  47 VLVDTGATTLCLVPEVISRLGLQLLKE-----VDVATAKGIGKARIFRDATLIIAGREGTFECLELPGG-QNNLLG 116
Cdd:cd00303   12 ALVDSGASVNFISESLAKKLGLPPRLLptplkVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDLLsYDVILG 87
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 48-116 4.43e-03

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 34.47  E-value: 4.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738449907   48 LVDTGATTLCLVPEVISRLGLQLL---KEVDVATAKGIGKARIFRDATLIIAGREGT-FECLELPGGQN-NLLG 116
Cdd:pfam13975  13 LVDTGASVTVISEALAERLGLDRLvdaYPVTVRTANGTVRAARVRLDSVKIGGIELRnVPAVVLPGDLDdVLLG 86
 
Name Accession Description Interval E-value
COG5550 COG5550
Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];
10-137 3.44e-15

Predicted aspartyl protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444293  Cd Length: 117  Bit Score: 67.21  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738449907  10 DMGKIYTSITVINRADQilaaaavispdqiRSLTLEnVLVDTGATT-LCLVPEVISRLGLQLLKEVDVATAKGIGKARIF 88
Cdd:COG5550    3 IMGEAFVEVEVIRLPDG-------------ESLEVD-ALVDTGFTGfLVLPSQLIEELGLPELGRRRARLADGSEVEFDV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 738449907  89 RDATLIIAGREGTFECLELPGGQNNLLGVIPLEALGLEPDLLSQKLRVL 137
Cdd:COG5550   69 YEATIEWDGQEAEVPVLAGDGITEPLLGVALLEGLGLVVDPIEGGLVLI 117
clan_AA_DTGF TIGR03698
clan AA aspartic protease, AF_0612 family; Members of this protein family are clan AA aspartic ...
 33-134 5.39e-09

clan AA aspartic protease, AF_0612 family; Members of this protein family are clan AA aspartic proteases, related to family TIGR02281. These proteins resemble retropepsins, pepsin-like proteases of retroviruses such as HIV. Members of this family are found in archaea and bacteria. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163410  Cd Length: 107  Bit Score: 50.82  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738449907   33 VISPDQIRSLTLeNVLVDTGATTLCLVP-EVISRLGLQLLKEVDVATAkgIGKARIFR--DATLIIAGREGTFECLELPG 109
Cdd:TIGR03698   6 LSNPKNPEFMEV-RALVDTGFSGFLLVPpDIVNKLGLPELDQRRVYLA--DGREVLTDvaKASIIINGLEIDAFVESLGY 82

                          90       100
                  ....*....|....*....|....*
gi 738449907  110 GQNNLLGVIPLEALGLEPDLLSQKL 134
Cdd:TIGR03698  83 VDEPLLGTELLEGLGIVIDYRNQGL 107
COG3577 COG3577
Predicted aspartyl protease [General function prediction only];
48-116 3.06e-04

Predicted aspartyl protease [General function prediction only];


Pssm-ID: 442797  Cd Length: 152  Bit Score: 38.78  E-value: 3.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738449907  48 LVDTGATTLCLVPEVISRLGLQ---LLKEVDVATAKGIGKARIFRDATLIIAG-REGTFECLELPGGQ--NNLLG 116
Cdd:COG3577   56 LVDTGASTVVLSESDARRLGLDpedLGRPVRVQTANGVVRAARVRLDSVRIGGiTLRNVRAVVLPGGEldDGLLG 130
retropepsin_like cd00303
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ...
 47-116 2.99e-03

Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133136  Cd Length: 92  Bit Score: 35.00  E-value: 2.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738449907  47 VLVDTGATTLCLVPEVISRLGLQLLKE-----VDVATAKGIGKARIFRDATLIIAGREGTFECLELPGG-QNNLLG 116
Cdd:cd00303   12 ALVDSGASVNFISESLAKKLGLPPRLLptplkVKGANGSSVKTLGVILPVTIGIGGKTFTVDFYVLDLLsYDVILG 87
gag-asp_proteas pfam13975
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ...
 48-116 4.43e-03

gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins.


Pssm-ID: 464060  Cd Length: 92  Bit Score: 34.47  E-value: 4.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738449907   48 LVDTGATTLCLVPEVISRLGLQLL---KEVDVATAKGIGKARIFRDATLIIAGREGT-FECLELPGGQN-NLLG 116
Cdd:pfam13975  13 LVDTGASVTVISEALAERLGLDRLvdaYPVTVRTANGTVRAARVRLDSVKIGGIELRnVPAVVLPGDLDdVLLG 86
Asp_protease_2 pfam13650
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ...
 46-117 6.26e-03

Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix.


Pssm-ID: 433378  Cd Length: 90  Bit Score: 34.18  E-value: 6.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738449907   46 NVLVDTGATTLCLVPEVISRLGLQLLKE---VDVATAKGIGKARIFRDATLIIAGREGT-FECLELPGGQN--NLLGV 117
Cdd:pfam13650  11 RFLVDTGASGTVISPSLAERLGLKVRGLaytVRVSTAGGRVSAARVRLDSLRLGGLTLEnVPALVLDLGDLidGLLGM 88
retropepsin_like_bacteria cd05483
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ...
 46-99 9.95e-03

Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133150  Cd Length: 96  Bit Score: 33.76  E-value: 9.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738449907  46 NVLVDTGATTLCLVPEVISRLGL--QLLKEVDVATAKGIGKARIFRDATLIIAGRE 99
Cdd:cd05483   15 RFLLDTGASTTVISEELAERLGLplTLGGKVTVQTANGRVRAARVRLDSLQIGGIT 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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